ID   EFG_CLOPA               Reviewed;          11 AA.
AC   P81350;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   02-JUN-2021, entry version 39.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
DE   AltName: Full=CP 5;
DE   Flags: Fragment;
GN   Name=fusA;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX   PubMed=9629918; DOI=10.1002/elps.1150190533;
RA   Flengsrud R., Skjeldal L.;
RT   "Two-dimensional gel electrophoresis separation and N-terminal sequence
RT   analysis of proteins from Clostridium pasteurianum W5.";
RL   Electrophoresis 19:802-806(1998).
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome changes
CC       from the pre-translocational (PRE) to the post-translocational (POST)
CC       state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC       deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC       coordinated movement of the two tRNA molecules, the mRNA and
CC       conformational changes in the ribosome (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC       G/EF-2 subfamily. {ECO:0000305}.
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DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..>11
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091108"
FT   NON_TER         11
SQ   SEQUENCE   11 AA;  1337 MW;  412E71F1D9C33B17 CRC64;
     KYPLEKFQNI G